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Database: UniProt
Entry: D5XAY4_THEPJ
LinkDB: D5XAY4_THEPJ
Original site: D5XAY4_THEPJ 
ID   D5XAY4_THEPJ            Unreviewed;       573 AA.
AC   D5XAY4;
DT   13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT   13-JUL-2010, sequence version 1.
DT   27-MAR-2024, entry version 49.
DE   SubName: Full=Aldehyde ferredoxin oxidoreductase {ECO:0000313|EMBL:ADG83338.1};
DE            EC=1.2.7.5 {ECO:0000313|EMBL:ADG83338.1};
GN   OrderedLocusNames=TherJR_2501 {ECO:0000313|EMBL:ADG83338.1};
OS   Thermincola potens (strain JR).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Thermincolaceae;
OC   Thermincola.
OX   NCBI_TaxID=635013 {ECO:0000313|EMBL:ADG83338.1, ECO:0000313|Proteomes:UP000002377};
RN   [1] {ECO:0000313|EMBL:ADG83338.1, ECO:0000313|Proteomes:UP000002377}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JR {ECO:0000313|EMBL:ADG83338.1,
RC   ECO:0000313|Proteomes:UP000002377};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Chertkov O., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA   Kyrpides N., Mikhailova N., Hazen T.C., Woyke T.;
RT   "Complete sequence of Thermincola sp. JR.";
RL   Submitted (MAY-2010) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000256|ARBA:ARBA00001966};
CC   -!- SIMILARITY: Belongs to the AOR/FOR family.
CC       {ECO:0000256|ARBA:ARBA00011032}.
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DR   EMBL; CP002028; ADG83338.1; -; Genomic_DNA.
DR   RefSeq; WP_013121332.1; NC_014152.1.
DR   AlphaFoldDB; D5XAY4; -.
DR   STRING; 635013.TherJR_2501; -.
DR   KEGG; tjr:TherJR_2501; -.
DR   eggNOG; COG2414; Bacteria.
DR   HOGENOM; CLU_020364_1_0_9; -.
DR   OrthoDB; 9763894at2; -.
DR   Proteomes; UP000002377; Chromosome.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0033726; F:aldehyde ferredoxin oxidoreductase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.569.10; Aldehyde Ferredoxin Oxidoreductase Protein, subunit A, domain 2; 1.
DR   Gene3D; 1.10.599.10; Aldehyde Ferredoxin Oxidoreductase Protein, subunit A, domain 3; 1.
DR   Gene3D; 3.60.9.10; Aldehyde ferredoxin oxidoreductase, N-terminal domain; 1.
DR   InterPro; IPR013984; Ald_Fedxn_OxRdtase_dom2.
DR   InterPro; IPR013985; Ald_Fedxn_OxRdtase_dom3.
DR   InterPro; IPR013983; Ald_Fedxn_OxRdtase_N.
DR   InterPro; IPR036503; Ald_Fedxn_OxRdtase_N_sf.
DR   InterPro; IPR001203; OxRdtase_Ald_Fedxn_C.
DR   InterPro; IPR036021; Tungsten_al_ferr_oxy-like_C.
DR   PANTHER; PTHR30038; ALDEHYDE FERREDOXIN OXIDOREDUCTASE; 1.
DR   PANTHER; PTHR30038:SF0; TUNGSTEN-CONTAINING ALDEHYDE FERREDOXIN OXIDOREDUCTASE; 1.
DR   Pfam; PF01314; AFOR_C; 1.
DR   Pfam; PF02730; AFOR_N; 1.
DR   SMART; SM00790; AFOR_N; 1.
DR   SUPFAM; SSF48310; Aldehyde ferredoxin oxidoreductase, C-terminal domains; 1.
DR   SUPFAM; SSF56228; Aldehyde ferredoxin oxidoreductase, N-terminal domain; 1.
PE   3: Inferred from homology;
KW   4Fe-4S {ECO:0000256|ARBA:ARBA00022485};
KW   Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000313|EMBL:ADG83338.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002377}.
FT   DOMAIN          1..205
FT                   /note="Aldehyde ferredoxin oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00790"
SQ   SEQUENCE   573 AA;  60853 MW;  2CA95CF9B7CB7CD7 CRC64;
     MKIYRVNMTN QTVTVEDVPA EWKGLGGRAL TSAIVGKEVE PTCHPLGKNN KLVIAPGLLS
     GTAAPNSGRL SVGAKSPLTG GIKESNAGGT AAQKLARLGI KALIIEGQPE GDKFYSIHVD
     KNGCRVQEEN ELVGKGNYEV VARLTEKFGS KIGVLTIGQA GETRMAAANI SVKDPDGNLR
     SAGRGGLGAV MGAKKVKYIT IDDAGAPGVA IADQEKFKEA ARRLAKGLRE HPVTGQGLPT
     YGTNVLVNII NEAGGLPTQN FRLGRYEHAN KISGETMHDI IVSRNGKPTH GCHAGCVIRC
     SQIYNDKDGN YLTAGFEYET IWGFGAHCCI DDLDIIAQAD RICDDIGIDS IETAVTMGVA
     MEGGVIPFGD GPGMLNLLKE IEQGTYLGRI LGNGAAFTGK ALGVTRVPVV KGQAMPAYDP
     RAVKGIGLTY ATSPMGADHT AGYSVATNVL KVGGEVNPLG KEGNIELSRN LQIATAALDS
     AGLCLFVAFC ILDNADAFQA IVDMINAQYG LNLTNDDITE LGKSVLRTER AFNEAAGFTR
     EHDRLPEFFR EECPPHNTTW DFTGEEIDTL YNF
//
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